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Deciphering environment effects in peptide bond solvation dynamics by experiment and theory

Please always quote using this URN: urn:nbn:de:bvb:20-opus-159647
  • Most proteins work in aqueous solution and the interaction with water strongly affects their structure and function. However, experimentally the motion of a specific single water molecule is difficult to trace by conventional methods, because they average over the heterogeneous solvation structure of bulk water surrounding the protein. Here, we provide a detailed atomistic picture of the water rearrangement dynamics around the –CONH– peptide linkage in the two model systems formanilide and acetanilide, which simply differ by the presence of aMost proteins work in aqueous solution and the interaction with water strongly affects their structure and function. However, experimentally the motion of a specific single water molecule is difficult to trace by conventional methods, because they average over the heterogeneous solvation structure of bulk water surrounding the protein. Here, we provide a detailed atomistic picture of the water rearrangement dynamics around the –CONH– peptide linkage in the two model systems formanilide and acetanilide, which simply differ by the presence of a methyl group at the peptide linkage. The combination of picosecond pump–probe time-resolved infrared spectroscopy and molecular dynamics simulations demonstrates that the solvation dynamics at the molecular level is strongly influenced by this small structural difference. The effective timescales for solvent migration triggered by ionization are mainly controlled by the efficiency of the kinetic energy redistribution rather than the shape of the potential energy surface. This approach provides a fundamental understanding of protein hydration and may help to design functional molecules in solution with tailored properties.show moreshow less
Metadaten
Author: Matthias Wohlgemuth, Mitsuhiko Miyazaki, Kohei Tsukada, Martin Weiler, Otto Dopfer, Masaaki Fujii, Roland MitrićORCiD
URN:urn:nbn:de:bvb:20-opus-159647
Document Type:Journal article
Faculties:Fakultät für Chemie und Pharmazie / Institut für Physikalische und Theoretische Chemie
Language:English
Parent Title (English):Physical Chemistry Chemical Physics
Year of Completion:2017
Volume:19
Issue:33
Pagenumber:22564-22572
Source:Physical Chemistry Chemical Physics, 2017,19, 22564-22572. DOI: 10.1039/C7CP03992A
URL:http://pubs.rsc.org/en/content/articlelanding/2017/cp/c7cp03992a
DOI:https://doi.org/10.1039/C7CP03992A
Sonstige beteiligte Institutionen:Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama 226-8503, Japan
Sonstige beteiligte Institutionen:Institut für Optik und Atomare Physik, Technische Universität Berlin, 10623 Berlin, Germany
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 54 Chemie / 541 Physikalische Chemie
Tag:hydration dynamics; infrared-spectra; protein hydration; trans-formanilide; water migration
PACS-Classification:30.00.00 ATOMIC AND MOLECULAR PHYSICS
Release Date:2018/03/23
Note:
Accepted Version
Embargo Date:2018/08/04
EU-Project number / Contract (GA) number:646737
OpenAIRE:OpenAIRE
Licence (German):License LogoDeutsches Urheberrecht